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Volumn 80, Issue 6, 2002, Pages 622-631

Enzymatic synthesis of amoxicillin: Avoiding limitations of the mechanistic approach for reaction kinetics

Author keywords

lactamic antibiotic; Artificial neural network; Hybrid model; Immobilized enzyme; Penicillin G acylase

Indexed keywords

ANTIBIOTICS; ENZYME KINETICS; NEURAL NETWORKS; SUBSTRATES;

EID: 0037146812     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10417     Document Type: Article
Times cited : (33)

References (25)
  • 1
    • 0021026006 scopus 로고
    • The penicillin acylase from Escherichia coli ATCC11105 consists of two dissimilar subunits
    • Böck A, Wirth R, Schmid G, Shumacher G, Lang G, Buckel P. 1983. The penicillin acylase from Escherichia coli ATCC11105 consists of two dissimilar subunits. FEMS Microbiol Lett 20:135-139.
    • (1983) FEMS Microbiol Lett , vol.20 , pp. 135-139
    • Böck, A.1    Wirth, R.2    Schmid, G.3    Shumacher, G.4    Lang, G.5    Buckel, P.6
  • 2
    • 0021930011 scopus 로고
    • Role of protein subunits in Proteus rettigeri penicillin G acylase
    • Daumy GO, Danley D, McColl A. 1985. Role of protein subunits in Proteus rettigeri penicillin G acylase. J Bacteriol 163:1279-1281.
    • (1985) J Bacteriol , vol.163 , pp. 1279-1281
    • Daumy, G.O.1    Danley, D.2    McColl, A.3
  • 5
    • 0028835759 scopus 로고
    • The use of stabilized penicillin acylase derivatives improves the design of kinetically controlled synthesis
    • Fernandez-Lafuente R, Rossel CM, Guisan JM. 1995. The use of stabilized penicillin acylase derivatives improves the design of kinetically controlled synthesis. J Mol Catal A 101:91-97.
    • (1995) J Mol Catal A , vol.101 , pp. 91-97
    • Fernandez-Lafuente, R.1    Rossel, C.M.2    Guisan, J.M.3
  • 7
    • 0037009219 scopus 로고    scopus 로고
    • The role of 6-aminopenicilanic acid on the kinetics of the enzymatic synthesis of amoxicillin catalyzed by penicillin g acylase immobilized on glyoxyl-agarose
    • in press
    • Gonçalves LRB, Fernandez-Lafuente R, Guisán JM, Giordano RLC. 2002a. The role of 6-aminopenicilanic acid on the kinetics of the enzymatic synthesis of amoxicillin catalyzed by penicillin g acylase immobilized on glyoxyl-agarose. Enzyme Microb Technol (in press).
    • (2002) Enzyme Microb Technol
    • Gonçalves, L.R.B.1    Fernandez-Lafuente, R.2    Guisán, J.M.3    Giordano, R.L.C.4
  • 9
    • 0024029957 scopus 로고
    • Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes
    • Guisan JM. 1988. Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes. Enzyme Microb Technol 10:375-382.
    • (1988) Enzyme Microb Technol , vol.10 , pp. 375-382
    • Guisan, J.M.1
  • 10
    • 0031055914 scopus 로고    scopus 로고
    • Review: Global and local neural network models in biotechnology: Application to different cultivation processes
    • Karim M, Yoshida NT, Rivera SL, Saucedo VM, Eikens B, Oh GS. 1997. Review: Global and local neural network models in biotechnology: Application to different cultivation processes. J Ferm Bioeng 83:1-11.
    • (1997) J Ferm Bioeng , vol.83 , pp. 1-11
    • Karim, M.1    Yoshida, N.T.2    Rivera, S.L.3    Saucedo, V.M.4    Eikens, B.5    Oh, G.S.6
  • 11
    • 0022630151 scopus 로고
    • Mechanism and yields in enzyme catalyzed equilibrium and kinetically controlled synthesis of β-lactam antibiotics, peptides and other condensation products
    • Kasche V. 1986. Mechanism and yields in enzyme catalyzed equilibrium and kinetically controlled synthesis of β-lactam antibiotics, peptides and other condensation products. Enzyme Microb Technol 8:4-16.
    • (1986) Enzyme Microb Technol , vol.8 , pp. 4-16
    • Kasche, V.1
  • 12
    • 0021672205 scopus 로고
    • Kinetic studies on the mechanism of the penicillin amidase-catalyzed synthesis of ampicillin and benzylpenicillin
    • Kasche V, Haufler U, Zöllner R. 1984. Kinetic studies on the mechanism of the penicillin amidase-catalyzed synthesis of ampicillin and benzylpenicillin. Hoppe-Seyler Physiol Chem 365:1435-1443.
    • (1984) Hoppe-Seyler Physiol Chem , vol.365 , pp. 1435-1443
    • Kasche, V.1    Haufler, U.2    Zöllner, R.3
  • 13
    • 0001404915 scopus 로고
    • Kinetics of acyl transfer by α-amino acid ester hydrolase from Xanthomonas citri
    • Kato K. 1980. Kinetics of acyl transfer by α-amino acid ester hydrolase from Xanthomonas citri. Agric Biol Chem 44:1083-1088.
    • (1980) Agric Biol Chem , vol.44 , pp. 1083-1088
    • Kato, K.1
  • 14
    • 0027112179 scopus 로고
    • Knowledge-based control of fermentation processes
    • Konstantinov KB, Yoshida T. 1992. Knowledge-based control of fermentation processes. Biotechnol Bioeng 39:479-486.
    • (1992) Biotechnol Bioeng , vol.39 , pp. 479-486
    • Konstantinov, K.B.1    Yoshida, T.2
  • 15
    • 0019174497 scopus 로고
    • Substrate specificity of penicillin amidase from Escherichia coli
    • Margolin AL, Svedas VKS, Berezin IV. 1980. Substrate specificity of penicillin amidase from Escherichia coli. Biochim Biophys Acta 616:283-289.
    • (1980) Biochim Biophys Acta , vol.616 , pp. 283-289
    • Margolin, A.L.1    Svedas, V.K.S.2    Berezin, I.V.3
  • 16
    • 0000169232 scopus 로고
    • An algorithm for least-square estimation of non-linear parameters
    • Marquardt DW. 1963. An algorithm for least-square estimation of non-linear parameters. J. Soc. Ind. Appl. Math. 11:431-441.
    • (1963) J Soc Ind Appl Math , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 18
    • 0035850792 scopus 로고    scopus 로고
    • Crystal structure of penicillin acylase enzyme-substrate complexes: Structural insights into the catalytic mechanism
    • McVey CE, Walsh MA, Dodson GG, Wilson KS, Brannigan JA. 2001. Crystal structure of penicillin acylase enzyme-substrate complexes: Structural insights into the catalytic mechanism. J Mol Biol 313:139-150.
    • (2001) J Mol Biol , vol.313 , pp. 139-150
    • McVey, C.E.1    Walsh, M.A.2    Dodson, G.G.3    Wilson, K.S.4    Brannigan, J.A.5
  • 21
    • 0018088319 scopus 로고
    • Substrate specificity of penicillin G acylase of E. coli
    • Plaskie A, Roets E, Vanderhaeghe H. 1978. Substrate specificity of penicillin G acylase of E. coli. J Antibiot 31:783-788.
    • (1978) J Antibiot , vol.31 , pp. 783-788
    • Plaskie, A.1    Roets, E.2    Vanderhaeghe, H.3
  • 22
    • 0022471098 scopus 로고
    • Learning representations by back-propagating errors
    • Rumelhart DE, Hinton GE, Williams RJ. 1986. Learning representations by back-propagating errors. Nature 323:533-536.
    • (1986) Nature , vol.323 , pp. 533-536
    • Rumelhart, D.E.1    Hinton, G.E.2    Williams, R.J.3
  • 24
    • 2242478862 scopus 로고    scopus 로고
    • Modeling is an indismissible tool to understand and control bioprocesses
    • Sonnleitner B, Cheruy A. 1997. Modeling is an indismissible tool to understand and control bioprocesses. J Biotechnol 52:173-174.
    • (1997) J Biotechnol , vol.52 , pp. 173-174
    • Sonnleitner, B.1    Cheruy, A.2
  • 25
    • 0034597401 scopus 로고    scopus 로고
    • Highly efficient synthesis of ampicillin in "aqueous solution-precipitate" systems. High substrate concentration and supersaturation effect
    • Youshko MI, Langen LM, Vroom E, Moody HM, Rantwijk F, Sheldon RA, Svedas VK. 2000. Highly efficient synthesis of ampicillin in "aqueous solution-precipitate" systems. High substrate concentration and supersaturation effect. J Mol Catal B: Enzymatic 10:509-515.
    • (2000) J Mol Catal B: Enzymatic , vol.10 , pp. 509-515
    • Youshko, M.I.1    Langen, L.M.2    Vroom, E.3    Moody, H.M.4    Rantwijk, F.5    Sheldon, R.A.6    Svedas, V.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.